The Structural Mechanisms of Chaperones and Their Applications in Medicine and Production

The structural formation and metabolic activities of organisms are inseparable from precise regulations of appropriate protein expression, processing, and modification. However, new-synthesized polypeptides or incompletely folded proteins in cells are prone to undirected misfolding and then aggregation, under external stress conditions. Many neurodegenerative diseases are intimately related to the aggregation of misfolded proteins in nerve cells. Importantly, molecular chaperones can specifically bind to substrates (including peptides and proteins) to stabilize their conformations to prevent aggregating, direct correct folding or refolding, promote disulfide-bond formation, and also regulate appropriate modifications such as phosphorylation. In addition, some chaperones mediate the localization of membrane proteins and extracellular secretion of proteins. Through a complete and thorough study of the complex interaction network between molecular chaperones and intracellular molecules, it is possible to provide reliable avenues and effective immune targets for therapies for cellular pathogen diseases. Some of them also serve as auxiliary factors for the efficacious delivery of protein drugs. Moreover, molecular chaperones play an important role in the artificial production of recombinant proteins, or rather, even indispensable. The artificial synthesis of chemical nanochaperones is a highly promising direction nowadays.